2Q8Y

Structural insight into the enzymatic mechanism of the phophothreonine lyase

2Q8Y の概要

• エントリーDOI: 10.2210/pdb2q8y/pdb
• 分子名称: 27.5 kDa virulence protein, Mitogen-activated protein kinase 7 (3 entities in total)
• 機能のキーワード: alpha/beta fold, lyase-transferase complex, lyase/transferase
• 由来する生物種: Salmonella enteritidis; 詳細
• 細胞内の位置: Cytoplasm: Q13164
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28934.28

構造登録者

Zhu, Y.-Q.,Wang, D.-C.,Shao, F. (登録日: 2007-06-12, 公開日: 2007-12-11, 最終更新日: 2024-10-09)

主引用文献

Zhu, Y.,Li, H.,Long, C.,Hu, L.,Xu, H.,Liu, L.,Chen, S.,Wang, D.C.,Shao, F.
Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase
Mol.Cell, 28:899-913, 2007

PubMed Abstract: The OspF family of phosphothreonine lyase, including SpvC from Salmonella, irreversibly inactivates the dual-phosphorylated host MAPKs (pT-X-pY) through beta elimination. We determined crystal structures of SpvC and its complex with a phosphopeptide substrate. SpvC adopts a unique fold of alpha/beta type. The disordered N terminus harbors a canonical D motif for MAPK substrate docking. The enzyme-substrate complex structure indicates that recognition of the phosphotyrosine followed by insertion of the threonine phosphate into an arginine pocket places the phosphothreonine into the enzyme active site. This requires the conformational flexibility of pT-X-pY, which suggests that p38 (pT-G-pY) is likely the preferred physiological substrate. Structure-based biochemical and enzymatic analysis allows us to propose a general acid/base mechanism for beta elimination reaction catalyzed by the phosphothreonine lyase. The mechanism described here provides a structural understanding of MAPK inactivation by a family of pathogenic effectors conserved in plant and animal systems and may also open a new route for biological catalysis.

PubMed: 18060821
DOI: 10.1016/j.molcel.2007.11.011

実験手法

X-RAY DIFFRACTION (2 Å)